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Database: UniProt
Entry: A0A0Q6PSV5_9MICO
LinkDB: A0A0Q6PSV5_9MICO
Original site: A0A0Q6PSV5_9MICO 
ID   A0A0Q6PSV5_9MICO        Unreviewed;       405 AA.
AC   A0A0Q6PSV5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=4-hydroxybenzoate 3-monooxygenase {ECO:0000313|EMBL:KQV07844.1};
DE            EC=1.14.13.2 {ECO:0000313|EMBL:KQV07844.1};
GN   ORFNames=ASC63_11715 {ECO:0000313|EMBL:KQV07844.1};
OS   Leifsonia sp. Root112D2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV07844.1, ECO:0000313|Proteomes:UP000051914};
RN   [1] {ECO:0000313|EMBL:KQV07844.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV07844.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV07844.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV07844.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQV07844.1}.
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DR   EMBL; LMCU01000001; KQV07844.1; -; Genomic_DNA.
DR   RefSeq; WP_055813437.1; NZ_LMCU01000001.1.
DR   AlphaFoldDB; A0A0Q6PSV5; -.
DR   STRING; 1736426.ASC63_11715; -.
DR   OrthoDB; 9791689at2; -.
DR   Proteomes; UP000051914; Unassembled WGS sequence.
DR   GO; GO:0018659; F:4-hydroxybenzoate 3-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43476; 3-(3-HYDROXY-PHENYL)PROPIONATE/3-HYDROXYCINNAMIC ACID HYDROXYLASE; 1.
DR   PANTHER; PTHR43476:SF4; BLR0106 PROTEIN; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Monooxygenase {ECO:0000313|EMBL:KQV07844.1};
KW   Oxidoreductase {ECO:0000313|EMBL:KQV07844.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051914}.
FT   DOMAIN          6..343
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   405 AA;  44315 MW;  D1EDD66526D991CA CRC64;
     MSAETTRVAI IGAGPAGLLL GWALRRSGID AIIVENRSVD YLLARVRAGV LEQGSVETLT
     RLGLGERLAS EGMIHDGIYL QFAGERHHVD FNELIGRTVT VYGQQAVVRD LLEAHEADGS
     TIYFEATDVS VHDIESRSPR VTFGHEGEAH EITADFIVGA DGFHGVCRPA IPAEAITMYD
     RSYPYAWLGI LASVAPSTDE LIYCLHEDGF AMHSMRSPQV SRLYLQVDPS ESIDEWSDAR
     IWDALQSRLG VPGWSLHAGE ITEKSITPMR SFVASTLNHG SLFLAGDAGH IVPPTGAKGL
     NSAISDVTML ADALIAHYAN DDTALTGYSD AALARQWRTQ QFSQWMTQML HRHPGDSHEL
     QFDYRSQLGQ LDYTTHSLHA MRSLAEQYTG LPLTTNGSTR GNIAL
//
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